Evidence map›Paper›PMID 24497982›Full record

ArticlePloS one2014

Molecular cloning, overexpression and characterization of a novel water channel protein from Rhodobacter sphaeroides.

Mustafa Erbakan, Yue-xiao Shen, Mariusz Grzelakowski, Peter J Butler, Manish Kumar, Wayne R Curtis

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
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  9. Highly permeable artificial water channels that can self-assemble into two-dimensional arrays.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Mustafa ErbakanDepartment of Biomedical Engineering, Pennsylvania State University, University Park, Pennsylvania, United States of America.
Yue-xiao ShenDepartment of Chemical Engineering, Pennsylvania State University, University Park, Pennsylvania, United States of America.
Mariusz GrzelakowskiAquaZ Inc, Cincinnati, Ohio, United States of America.
Peter J ButlerDepartment of Biomedical Engineering, Pennsylvania State University, University Park, Pennsylvania, United States of America.
Manish KumarDepartment of Chemical Engineering, Pennsylvania State University, University Park, Pennsylvania, United States of America.
Wayne R CurtisDepartment of Biomedical Engineering, Pennsylvania State University, University Park, Pennsylvania, United States of America ; Department of Chemical Engineering, Pennsylvania State University, University Park, Pennsylvania, United States of America.
Pennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aquaporins are highly selective water channel proteins integrated into plasma membranes of single cell organisms; plant roots and stromae; eye lenses, renal and red blood cells in vertebrates. To date, only a few microbial aquaporins have been characterized and their physiological importance is not well understood. Here we report on the cloning, expression and characterization of a novel aquaporin, RsAqpZ, from a purple photosynthetic bacterium, Rhodobacter sphaeroides ATCC 17023. The protein was expressed homologously at a high yield (∼20 mg/L culture) under anaerobic photoheterotrophic growth conditions. Stopped-flow light scattering experiments demonstrated its high water permeability (0.17±0.05 cm/s) and low energy of activation for water transport (2.93±0.60 kcal/mol) in reconstituted proteoliposomes at a protein to lipid ratio (w/w) of 0.04. We developed a fluorescence correlation spectroscopy based technique and utilized a fluorescent protein fusion of RsAqpZ, to estimate the single channel water permeability of RsAqpZ as 1.24 (±0.41) x 10(-12) cm(3)/s or 4.17 (±1.38)×10(10) H2O molecules/s, which is among the highest single channel permeability reported for aquaporins. Towards application to water purification technologies, we also demonstrated functional incorporation of RsAqpZ in amphiphilic block copolymer membranes.

Indexed as

AlgorithmsAmino Acid SequenceAquaporinsBacterial ProteinsBiological TransportBlotting, WesternCell Membrane PermeabilityCloning, MolecularGene Expression Regulation, BacterialLiposomesLuminescent ProteinsMicroscopy, ElectronModels, BiologicalMolecular Sequence DataPhylogenyRecombinant ProteinsAquaporinsBacterial ProteinsLiposomesLuminescent ProteinsRecombinant ProteinsWater

Identifiers

PMID24497982
PMCPMC3909002
OpenAlexW2037812012

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.